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Most bacterial cytochrome P450 monooxygenases (P450s or CYPs) require two redox partner proteins for activity. To reduce complexity of the redox chain, the  Bacillus subtilis  flavodoxin YkuN (Y) was fused to the  Escherichia coli  flavodoxin reductase Fpr (R), and activity was tuned by placing flexible (GGGGS) n  or rigid ([E/L]PPPP) n  linkers (n = 1–5) in between. P-linker constructs typically outperformed their G-linker counterparts, with superior performance of YR-P5, which carries linker ([E/L]PPPP) 5 . Molecular dynamics simulations demonstrated that ([E/L]PPPP) n  linkers are intrinsically rigid, whereas (GGGGS) n  linkers are highly flexible and biochemical experiments suggest a higher degree of separation between the fusion partners in case of long rigid P-linkers. The catalytic properties of the individual redox partners were best preserved in the YR-P5 construct. In comparison to the separate redox partners, YR-P5 exhibited attenuated rates of NADPH oxidation and heme iron (III) reduction, while coupling efficiency was improved (28%  vs . 49% coupling with  B. subtilis  CYP109B1, and 44%  vs . 50% with  Thermobifida fusca  CYP154E1). In addition, YR-P5 supported monooxygenase activity of the CYP106A2 from  Bacillus megaterium  and bovine CYP21A2. The versatile YR-P5 may serve as a non-physiological electron transfer system for exploitation of the catalytic potential of other P450s.

Engineering of versatile redox partner fusions that support monooxygenase activity of functionally diverse cytochrome P450s